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Objective: Heparin-binding epidermal growth factor (EGF)-like growth factor (HB-EGF), which binds to the EGF receptor, plays an important role in the occurrence and development of inflammation in various diseases. HB-EGF mediates the progression of ovarian cancer and is associated with disease prognosis. Thus, a specific humanized antibody to HB-EGF with high affinity is important. Methods: In this study, a humanized domain antibody (VH) against HB-EGF was discovered through phage display technology. The domain antibody was expressed in HB2151 cells and purified from the supernatant using protein L, and were used to test the its effect in invasion and migration of ovarian cancer SKOV3. Results: A domain antibody against HB-EGF was discovered, with a dissociation constant of ∼30 nM. Functional assays indicated that the domain antibody inhibited the functions of HB-EGF in promoting invasion and migration of SKOV3 cells. Conclusions: The selected domain antibody is a potential tool for developing novel drugs or therapies to combat ovarian cancer. [ABSTRACT FROM AUTHOR]

Heparin-binding epidermal growth factor-like growth factor (HB-EGF) belongs to the EGF family and exhibits its activity after binding to its receptors in autocrine, paracrine, and juxtacrine interactions. HB-EGF plays important roles in several biological and pathological processes, such as wound healing, blastocyst implantation, atherosclerosis, and heart development. Clinical studies have shown that HB-EGF is closely correlated with tumorigenesis, metastasis, and drug resistance in breast cancer. Specifically, targeted inhibition of HB-EGF improves the therapeutic efficacy and suppresses the tumor progression. This review discusses the importance of HB-EGF in mammary carcinoma progression and the potential value of HB-EGF as a therapeutic target for breast cancer treatment. [ABSTRACT FROM AUTHOR]